Cleaning and/or treatment compositions

ABSTRACT

This invention relates to compositions comprising certain amylase variants and processes for making and using such compositions including the use of such compositions to clean and/or treat a situs.

CROSS-REFERENCES TO RELATED APPLICATIONS

This application claims priority under 35 U.S.C. § 120 to U.S.application Ser. No. 11/811,129 filed Jun. 8, 2007, which in turn claimspriority under 35 U.S.C. § 119(e) to U.S. Provisional Application Ser.No. 60/814,442 filed Jun. 16, 2006.

FIELD OF INVENTION

Compositions comprising enzymes and processes for making and using suchcompositions.

BACKGROUND OF THE INVENTION

The appearance of enzymes suitable for cleaning and/or treatmentapplications gave the formulator a new approach to clean and/or treathard surfaces and fabrics. Unfortunately, even when enzymes areemployed, performance issues remain. For example, in certain matricesand/or use conditions, enzymes do not deposit as efficiently as requiredto provide the desired performance. Thus, the use of this technologycontinues to be limited.

Surprisingly, when cleaning compositions that comprise certainα-amylases are formulated in accordance with the teachings of thepresent invention, such compositions can provide improved cleaning.

SUMMARY OF THE INVENTION

This invention relates to compositions comprising certain α-amylaseenzymes and processes for making and using such products.

DETAILED DESCRIPTION OF THE INVENTION Definitions

As used herein, the term “cleaning composition” includes, unlessotherwise indicated, granular or powder-form all-purpose or “heavy-duty”washing agents, especially laundry detergents; liquid, gel or paste-formall-purpose washing agents, especially the so-called heavy-duty liquidtypes; liquid fine-fabric detergents; hand dishwashing agents or lightduty dishwashing agents, especially those of the high-foaming type;machine dishwashing agents, including the various tablet, granular,liquid and rinse-aid types for household and institutional use; liquidcleaning and disinfecting agents, including antibacterial hand-washtypes, laundry bars, mouthwashes, denture cleaners, car or carpetshampoos, bathroom cleaners; hair shampoos and hair-rinses; shower gelsand foam baths and metal cleaners; as well as cleaning auxiliaries suchas bleach additives and “stain-stick” or pre-treat types.

As used herein, the phrase “is independently selected from the groupconsisting of . . . ” means that moieties or elements that are selectedfrom the referenced Markush group can be the same, can be different orany mixture of elements.

As used herein, articles, for example, “a” and “an” when used in aclaim, are understood to mean one or more of what is claimed ordescribed.

As used herein, the terms “include”, “includes” and “including” aremeant to be non-limiting.

The test methods disclosed in the Test Methods Section of the presentapplication must be used to determine the respective values of theparameters of Applicants' inventions.

Unless otherwise noted, all component or composition levels are inreference to the active level of that component or composition, and areexclusive of impurities, for example, residual solvents or by-products,which may be present in commercially available sources.

Unless otherwise noted, the enzymes of the present invention areexpressed in terms of active protein level and are exclusive ofimpurities, for example, residual solvents or by-products, which may bepresent in commercially available sources.

All percentages and ratios are calculated by weight unless otherwiseindicated. All percentages and ratios are calculated based on the totalcomposition unless otherwise indicated.

It should be understood that every maximum numerical limitation giventhroughout this specification includes every lower numerical limitation,as if such lower numerical limitations were expressly written herein.Every minimum numerical limitation given throughout this specificationwill include every higher numerical limitation, as if such highernumerical limitations were expressly written herein. Every numericalrange given throughout this specification will include every narrowernumerical range that falls within such broader numerical range, as ifsuch narrower numerical ranges were all expressly written herein.

Compositions

In one aspect, a composition comprising an amylase and:

-   -   a.) a sufficient amount of calcium to provide a wash liquor        comprising said composition with a free calcium concentration as        determined by Test Method 1 of from about 0.1 ppm to about 500        ppm, from about 0.2 ppm to about 200 ppm, from about 1 ppm to        about 150 ppm, or from about 2 ppm to about 100 ppm, or even        from about 3 ppm to about 50 ppm;    -   b.) based on total product weight, less than 15%, less than 10%,        less than 8% or even from about 0.01% to about 7% builder;        and/or    -   c.) having an enzyme deposition index as defined in Test Method        2 of at least 2.5, at least 2.6, or even from about 2.7 to about        50 is disclosed.        Such composition may comprise, based on total composition        weight, from about 0.0001% to about 2%, from about 0.0005% to        about 1%, from about 0.001% to about 0.5% or even from about        0.002% to about 0.25% of said enzyme. Such compositions may be        cleaning and/or treatment compositions. Thus it is understood        that they may be solids or fluids.

In one aspect, said amylase includes α-amylases derived from Bacilluslicheniformis having Sequence I.D. 5 or 6, or an enzyme that is at least65%, 70%, 75%, 80%, 85%, 90%, 95%, or even 99% identical to saidSequence I.D. 5 or 6. Such α-amylases having at least one of thefollowing mutations at positions corresponding to the positionscorresponding to Sequence I.D. 5 or 6: 15, 23, 133, 188, 209, 475 orcombinations of said positions.

In another aspect, said amylase enzymes include α-amylases derived fromBacillus licheniformis having Sequence I.D. 5 (SEQ ID No. 5 herein beingequivalent to SEQ ID No 34 in U.S. Pat. No. 5,958,739) or an enzymehaving at least 65%, 70%, 75%, 80%, 85%, 90%, 95%, or even 99% identityto said Sequence I.D. 5. Such α-amylases having one or more of thefollowing mutations: M15T, H133Y, N188S or T, A209V or G475R.

In another aspect, said amylase enzymes include α-amylases derived fromBacillus licheniformis having Sequence 6 (SEQ ID No. 6 herein beingequivalent to SEQ ID NO. 2 in U.S. Pat. No. 6,436,888 B1) or an enzymehaving at least 65%, 70%, 75%, 80%, 85%, 90%, 95%, or even 99% identityto said Sequence I.D. 6. Such α-amylases having one or more of thefollowing mutations: M15T, H133Y, N188S or T, A209V or G475R; andoptionally R23K.

In another aspect, said amylase enzymes include an amylase selected fromthe group consisting of:

-   -   a.) an amylase having Seq. I.D. 5, said amylase having one of        the following groups of mutations:        -   (i) M15T+H133Y+N188S+A209V;        -   (ii) M15T+H133Y+N188T+A209V;        -   (iii) H133Y+N188S+G475R; or        -   (iv) H133Y+N188S;    -   b.) an amylase having Seq. I.D. 6, said amylase having one of        the following groups of mutations:        -   (i) M15T+R23K+H133Y+N188S+A209V;        -   (ii) M15T+R23K+H133Y+N188T+A209V;        -   (iii) R23K+H133Y+N188S+G475R;        -   (iv) R23K+H133Y+N188S;        -   (v) M15T+H133Y+N188S+A209V        -   (vi) M15T+H133Y+N188T+A209V;        -   (vii) H133Y+N188S+G475R; or        -   (viii) H133Y+N188S            and combinations thereof.

In one aspect, a composition comprising an amylase belonging to EC3.2.1.1 such as an enzyme having Seq. I.D. 1 and:

-   -   a.) a sufficient amount of calcium to provide a wash liquor        comprising said composition with a free calcium concentration as        determined by Test Method 1 of from about 0.1 ppm to about 500        ppm, from about 0.2 ppm to about 200 ppm, from about 1 ppm to        about 150 ppm, or from about 2 ppm to about 100 ppm, or even        from about 3 ppm to about 50 ppm;    -   b.) based on total product weight, less than 15%, less than 10%,        less than 8% or even from about 0.01% to about 7% builder;        and/or    -   c.) having an enzyme deposition index as defined in Test Method        2 of at least 2.5, at least 2.6, or even from about 2.7 to about        50 is disclosed.        Such composition may comprise, based on total composition        weight, from about 0.0001% to about 2%, from about 0.0005% to        about 1%, from about 0.001% to about 0.5% or even from about        0.002% to about 0.25% of said enzyme. Such compositions may be        cleaning and/or treatment compositions. Thus it is understood        that they may be solids or fluids.

Any of the aspects of said compositions described in the presentspecification may comprise a material selected from the group consistingof surfactants, builders, chelating agents, dye transfer inhibitingagents, dispersants, additional enzymes, and enzyme stabilizers,catalytic materials, bleaching agents, polymeric dispersing agents, claysoil removal/anti-redeposition agents, brighteners, suds suppressors,dyes, perfumes, structure elasticizing agents, fabric softeners,carriers, hydrotropes, processing aids, solvents, pigments, hueingagents, structurants, and mixtures thereof.

Any of the aspects of said compositions described in the presentspecification may comprise an additional enzyme selected from the groupconsisting of hemicellulases, peroxidases, proteases, cellulases,xylanases, lipases, phospholipases, esterases, cutinases, pectinases,mannanases, pectate lyases, keratinases, reductases, oxidases,phenoloxidases, lipoxygenases, ligninases, pullulanases, tannases,pentosanases, glucanases, arabinosidases, hyaluronidase, chondroitinase,laccase, amylases, or mixtures thereof.

In one aspect, such additional enzyme may be selected from the groupconsisting of: lipases, including “first cycle lipases” described inU.S. Pat. No. 6,939,702 B1 (SEQ ID No. 2 in the present specificationbeing equivalent to SEQ ID NO:1 in U.S. Pat. No. 6,939,702 B1), avariant of SEQ ID No. 2, a variant of SEQ ID No. 2 having at least 90%identity to SEQ ID No. 2 comprising a substitution of an electricallyneutral or negatively charged amino acid with R or K at any of positions3, 224, 229, 231 and 233, or even a variant comprising T231R and N233Rmutations, such variant being sold under the tradename Lipex®;alpha-amylases, including a variant of SEQ ID No. 3 (SEQ ID No. 3corresponding to SEQ ID No. 2 in U.S. Pat. No. 5,856,164), a variant ofSEQ ID No. 3 having at least 90% identity to SEQ ID No. 3 (such variantdisclosed in U.S. Pat. No. 6,187,576) comprising two deletions atpositions 183 and 184 and sold under the tradename Natalase®; serineproteases, including neutral or alkaline microbial serine proteases,such as subtilisins (EC 3.4.21.62), including those derived fromBacillus lentus, B. alkalophilus, B. subtilis, B. amyloliquefaciensdescribed in U.S. Pat. No. 6,312,936 B1, U.S. Pat. No. 5,679,630, U.S.Pat. No. 4,760,025; microbial-derived endoglucanases exhibitingendo-beta-1,4-glucanase activity (E.C. 3.2.1.4), including a bacterialpolypeptide endogenous to a member of the genus Bacillus which has asequence of at least 90%, 94%, 97% and even 99% identity to the aminoacid sequence of SEQ ID No. 4 (SEQ ID No. 4 herein being equivalent toSEQ ID NO:2 in US 2005/0112749 A1)—such an enzyme being commerciallyavailable under the tradename Celluclean™ by Novozymes A/S, and mixturesthereof.

Any of the aspects of the compositions described in the presentspecification may comprise a surfactant, including a surfactant selectedfrom the group of anionic surfactants including anionic surfactantsselected from the group consisting of linear alkylbenzene-sulfonate(LAS), alcohol ethoxysulfate (AES), mid-branched alkyl sulfates (HSAS)and mixtures thereof; non-ionic surfactants including alcoholethoxylates, for example alcohol ethoxylates having a chain length offrom 1 to 14 carbons, or 12 to 14 carbons; amine oxides and mixturesthereof.

Any of the aspects of the compositions described in the presentspecification may comprise a polymer, including polymers selected fromthe group consisting of polyacrylates, maleic/acrylic acid copolymers,cellulose-derived polymers, including carboxymethylcellulose and methylhydroxyethylcellulose, polyethyleneimine polymers and mixtures thereof.

Any of the aspects of said compositions described in the presentspecification may comprise a builder selected from the group consistingof citric acid, C₁₂-C₁₈ fatty acid, aluminosilicates, including zeolitesA, X and/or Y, sodium tripolyphosphate and mixtures thereof.

Any of the aspects of the compositions described in the presentspecification may comprise a material selected from the group consistingof a photobleach, a fabric hueing agent and mixtures thereof.

Any of the aspects of the compositions described in the presentspecification may comprise a photobleach being selected from the groupconsisting of xanthene dyes and mixtures thereof; sulfonated zincphthalocyanine, sulfonated aluminum phthalocyanine, Eosin Y, Phoxine B,Rose Bengal, C.I. Food Red 14 and mixtures thereof; water solublephthalocyanine; and/or a fabric hueing agent selected from the groupconsisting of dyes, including small molecule dyes such as small moleculedyes selected from the group consisting of Colour Index (Society ofDyers and Colourists, Bradford, UK) numbers Direct Violet 9, DirectViolet 35, Direct Violet 48, Direct Violet 51, Direct Violet 66, DirectBlue 1, Direct Blue 71, Direct Blue 80, Direct Blue 279, Acid Red 17,Acid Red 73, Acid Red 88, Acid Red 150, Acid Violet 15, Acid Violet 17,Acid Violet 24, Acid Violet 43, Acid Violet 49, Acid Blue 15, Acid Blue17, Acid Blue 25, Acid Blue 29, Acid Blue 40, Acid Blue 45, Acid Blue75, Acid Blue 80, Acid Blue 83, Acid Blue 90 and Acid Blue 113, AcidBlack 1, Basic Violet 1, Basic Violet 3, Basic Violet 4, Basic Violet10, Basic Violet 35, Basic Blue 3, Basic Blue 16, Basic Blue 22, BasicBlue 47, Basic Blue 66, Basic Blue 75, Basic Blue 159 and mixturesthereof, polymeric dyes and mixtures thereof, dye-clay conjugatescomprising at least one cationic/basic dye and a smectite clay andmixtures thereof.

Any of the aspects of the compositions described in the presentspecification may comprise, based on total product weight, from about 0%to about 3%, from about 0.0001% to about 0.5%, or even from about0.0005% to about 0.3% photobleach and/or from about 0.00003% to about0.3%, from about 0.00008% to about 0.05%, or even from about 0.0001% toabout 0.04% hueing agent.

Enzymes suitable for use in the present compositions can be obtainedfrom Genencor International, Palo Alto, Calif., U.S.A; Novozymes A/S,Bagsvaerd, Denmark; Amersham Pharmacia Biotech., Piscataway, N.J.,U.S.A; Sigma-Aldrich Company Ltd, Dorset, UK.

An enzyme having Seq. ID 1 is sold under the tradename Optisize® HT Plusby Genencor International, Palo Alto, Calif., U.S.A. An enzyme having atleast 90% identity to Seq. ID 2 is sold under the tradename Lipex® byNovozymes A/S, Bagsvaerd, Denmark. An enzyme having at least 90%identity with Seq. ID 3 is sold under the tradename Natalase® byNovozymes A/S, Bagsvaerd, Denmark. An enzyme having at least 90%identity to Seq. ID 4 is sold under the tradename Celluclean™ byNovozymes A/S, Bagsvaerd, Denmark. An enzyme having Seq. ID 5 is soldunder the tradename of Purastar® by Genencor International, Palo Alto,Calif., U.S.A. An enzyme having Seq. ID 6 is sold under the tradename ofTermamyl® by Novozymes A/S, Bagsvaerd, Denmark.

Surfactants suitable for use in the present compositions can be obtainedfrom Stepan, Northfield, Ill., USA; Huntsman, Salt Lake City, Utah, USA;Procter & Gamble Chemicals, Cincinnati, Ohio, USA.

Builders suitable for use in the present compositions can be obtainedfrom Rhodia, Paris, France; Industrial Zeolite (UK) Ltd, Grays, Essex,UK; Koma, Nestemica, Czech Republic.

Polymers suitable for use in the present compositions can be obtainedfrom BASF, Ludwigshafen, Germany, CP Kelco, Arnhem, Netherlands.

Photobleaches suitable for use in the present compositions can beobtained from Aldrich, Milwaukee, Wis., USA; Frontier Scientific, Logan,Utah, USA; Ciba Specialty Chemicals, Basel, Switzerland; BASF,Ludwigshafen, Germany; Lamberti S.p.A, Gallarate, Italy; Dayglo ColorCorporation, Mumbai, India; Organic Dyestuffs Corp., East Providence,R.I., USA.

Hueing agents suitable for use in the present compositions can beobtained from Aldrich, Milwaukee, Wis., USA; Ciba Specialty Chemicals,Basel, Switzerland; BASF, Ludwigshafen, Germany; Dayglo ColorCorporation, Mumbai, India; Organic Dyestuffs Corp., East Providence,R.I., USA; Dystar, Frankfurt, Germany; Lanxess, Leverkusen, Germany;Megazyme, Wicklow, Ireland; Clariant, Muttenz, Switzerland.

Adjunct Materials

While not essential for the purposes of the present invention, thenon-limiting list of adjuncts illustrated hereinafter are suitable foruse in the instant compositions and may be desirably incorporated incertain embodiments of the invention, for example to assist or enhancecleaning performance, for treatment of the substrate to be cleaned, orto modify the aesthetics of the cleaning composition as is the case withperfumes, colorants, dyes or the like. The precise nature of theseadditional components, and levels of incorporation thereof, will dependon the physical form of the composition and the nature of the cleaningoperation for which it is to be used. Suitable adjunct materialsinclude, but are not limited to, additional surfactants, additionalbuilders, additional polymers, additional hueing agents, additionalphotobleaches, chelating agents, dye transfer inhibiting agents,dispersants, additional enzymes, and enzyme stabilizers, catalyticmaterials, bleach activators, hydrogen peroxide, sources of hydrogenperoxide, preformed peracids, polymeric dispersing agents, clay soilremoval/anti-redeposition agents, brighteners, suds suppressors, dyes,perfumes, structure elasticizing agents, fabric softeners, carriers,hydrotropes, processing aids, solvents, additional hueing agents,structurants and/or pigments. In addition to the disclosure below,suitable examples of such other adjuncts and levels of use are found inU.S. Pat. Nos. 5,576,282, 6,306,812 B1 and 6,326,348 B1 that areincorporated by reference.

As stated, the adjunct ingredients are not essential to Applicants'compositions. Thus, certain embodiments of Applicants' compositions donot contain one or more of the following adjuncts materials: additionalsurfactants, additional builders, additional polymers, additionalphotobleaches, chelating agents, dye transfer inhibiting agents,dispersants, additional enzymes, and enzyme stabilizers, catalyticmaterials, bleach activators, hydrogen peroxide, sources of hydrogenperoxide, preformed peracids, polymeric dispersing agents, clay soilremoval/anti-redeposition agents, brighteners, suds suppressors, dyes,perfumes, structure elasticizing agents, fabric softeners, carriers,hydrotropes, processing aids, solvents, additional hueing agents,structurants and/or pigments. However, when one or more adjuncts arepresent, such one or more adjuncts may be present as detailed below:

Bleaching Agents—The cleaning compositions of the present invention maycomprise one or more bleaching agents. Suitable bleaching agents otherthan bleaching catalysts include photobleaches, bleach activators,hydrogen peroxide, sources of hydrogen peroxide, pre-formed peracids andmixtures thereof. In general, when a bleaching agent is used, thecompositions of the present invention may comprise from about 0.1% toabout 50% or even from about 0.1% to about 25% bleaching agent by weightof the subject cleaning composition. Examples of suitable bleachingagents include:

(1) photobleaches

(2) preformed peracids: Suitable preformed peracids include, but are notlimited to, compounds selected from the group consisting ofpercarboxylic acids and salts, percarbonic acids and salts, perimidicacids and salts, peroxymonosulfuric acids and salts, for example,Oxone®, and mixtures thereof. Suitable percarboxylic acids includehydrophobic and hydrophilic peracids having the formula R—(C═O)O—O-Mwherein R is an alkyl group, optionally branched, having, when theperacid is hydrophobic, from 6 to 14 carbon atoms, or from 8 to 12carbon atoms and, when the peracid is hydrophilic, less than 6 carbonatoms or even less than 4 carbon atoms; and M is a counter ion, forexample, sodium, potassium or hydrogen;

(3) sources of hydrogen peroxide, for example, inorganic perhydratesalts, including alkali metal salts such as sodium salts of perborate(usually mono- or tetra-hydrate), percarbonate, persulphate,perphosphate, persilicate salts and mixtures thereof. In one aspect ofthe invention the inorganic perhydrate salts are selected from the groupconsisting of sodium salts of perborate, percarbonate and mixturesthereof. When employed, inorganic perhydrate salts are typically presentin amounts of from 0.05 to 40 wt %, or 1 to 30 wt % of the overallcomposition and are typically incorporated into such compositions as acrystalline solid that may be coated. Suitable coatings include,inorganic salts such as alkali metal silicate, carbonate or borate saltsor mixtures thereof, or organic materials such as water-soluble ordispersible polymers, waxes, oils or fatty soaps; and

(4) bleach activators having R—(C═O)-L wherein R is an alkyl group,optionally branched, having, when the bleach activator is hydrophobic,from 6 to 14 carbon atoms, or from 8 to 12 carbon atoms and, when thebleach activator is hydrophilic, less than 6 carbon atoms or even lessthan 4 carbon atoms; and L is leaving group. Examples of suitableleaving groups are benzoic acid and derivatives thereof—especiallybenzene sulphonate. Suitable bleach activators include dodecanoyloxybenzene sulphonate, decanoyl oxybenzene sulphonate, decanoyloxybenzoic acid or salts thereof, 3,5,5-trimethyl hexanoyloxybenzenesulphonate, tetraacetyl ethylene diamine (TAED) and nonanoyloxybenzenesulphonate (NOBS). Suitable bleach activators are also disclosed in WO98/17767. While any suitable bleach activator may be employed, in oneaspect of the invention the subject cleaning composition may compriseNOBS, TAED or mixtures thereof.

When present, the peracid and/or bleach activator is generally presentin the composition in an amount of from about 0.1 to about 60 wt %, fromabout 0.5 to about 40 wt % or even from about 0.6 to about 10 wt % basedon the composition. One or more hydrophobic peracids or precursorsthereof may be used in combination with one or more hydrophilic peracidor precursor thereof.

The amounts of hydrogen peroxide source and peracid or bleach activatormay be selected such that the molar ratio of available oxygen (from theperoxide source) to peracid is from 1:1 to 35:1, or even 2:1 to 10:1.

Surfactants—The cleaning compositions according to the present inventionmay comprise a surfactant or surfactant system wherein the surfactantcan be selected from nonionic surfactants, anionic surfactants, cationicsurfactants, ampholytic surfactants, zwitterionic surfactants,semi-polar nonionic surfactants and mixtures thereof. When present,surfactant is typically present at a level of from about 0.1% to about60%, from about 1% to about 50% or even from about 5% to about 40% byweight of the subject composition.

Builders—The cleaning compositions of the present invention may compriseone or more detergent builders or builder systems. Builders include, butare not limited to, the alkali metal, ammonium and alkanolammonium saltsof polyphosphates, alkali metal silicates, alkaline earth and alkalimetal carbonates, aluminosilicate builders and polycarboxylatecompounds, ether hydroxypolycarboxylates, copolymers of maleic anhydridewith ethylene or vinyl methyl ether, 1,3,5-trihydroxybenzene-2,4,6-trisulphonic acid, and carboxymethyloxysuccinic acid, thevarious alkali metal, ammonium and substituted ammonium salts ofpolyacetic acids such as ethylenediamine tetraacetic acid andnitrilotriacetic acid, as well as polycarboxylates such as melliticacid, succinic acid, citric acid, oxydisuccinic acid, polymaleic acid,benzene 1,3,5-tricarboxylic acid, carboxymethyloxysuccinic acid, andsoluble salts thereof.

Chelating Agents—The cleaning compositions herein may contain achelating agent. Suitable chelating agents include copper, iron and/ormanganese chelating agents and mixtures thereof. When a chelating agentis used, the subject composition may comprise from about 0.005% to about15% or even from about 3.0% to about 10% chelating agent by weight ofthe subject composition.

Dye Transfer Inhibiting Agents—The cleaning compositions of the presentinvention may also include one or more dye transfer inhibiting agents.Suitable polymeric dye transfer inhibiting agents include, but are notlimited to, polyvinylpyrrolidone polymers, polyamine N-oxide polymers,copolymers of N-vinylpyrrolidone and N-vinylimidazole,polyvinyloxazolidones and polyvinylimidazoles or mixtures thereof. Whenpresent in a subject composition, the dye transfer inhibiting agents maybe present at levels from about 0.0001% to about 10%, from about 0.01%to about 5% or even from about 0.1% to about 3% by weight of thecomposition.

Brighteners—The cleaning compositions of the present invention can alsocontain additional components that may tint articles being cleaned, suchas fluorescent brighteners. Suitable fluorescent brightener levelsinclude lower levels of from about 0.01, from about 0.05, from about 0.1or even from about 0.2 wt % to upper levels of 0.5 or even 0.75 wt %.

Dispersants—The compositions of the present invention can also containdispersants. Suitable water-soluble organic materials include the homo-or co-polymeric acids or their salts, in which the polycarboxylic acidcomprises at least two carboxyl radicals separated from each other bynot more than two carbon atoms.

Enzymes—The cleaning compositions can comprise one or more enzymes whichprovide cleaning performance and/or fabric care benefits. Examples ofsuitable enzymes include, but are not limited to, hemicellulases,peroxidases, proteases, cellulases, xylanases, lipases, phospholipases,esterases, cutinases, pectinases, mannanases, pectate lyases,keratinases, reductases, oxidases, phenoloxidases, lipoxygenases,ligninases, pullulanases, tannases, pentosanases, glucanases,arabinosidases, hyaluronidase, chondroitinase, laccase, amylases, ormixtures thereof. A typical combination is an enzyme cocktail that maycomprise, for example, a protease and lipase in conjunction withamylase. When present in a cleaning composition, the aforementionedadditional enzymes may be present at levels from about 0.00001% to about2%, from about 0.0001% to about 1% or even from about 0.001% to about0.5% enzyme protein by weight of the composition.

Enzyme Stabilizers—Enzymes for use in detergents can be stabilized byvarious techniques. The enzymes employed herein can be stabilized by thepresence of water-soluble sources of calcium and/or magnesium ions inthe finished compositions that provide such ions to the enzymes. In caseof aqueous compositions comprising protease, a reversible proteaseinhibitor, such as a boron compound, can be added to further improvestability.

Catalytic Metal Complexes—Applicants' cleaning compositions may includecatalytic metal complexes. One type of metal-containing bleach catalystis a catalyst system comprising a transition metal cation of definedbleach catalytic activity, such as copper, iron, titanium, ruthenium,tungsten, molybdenum, or manganese cations, an auxiliary metal cationhaving little or no bleach catalytic activity, such as zinc or aluminumcations, and a sequestrate having defined stability constants for thecatalytic and auxiliary metal cations, particularlyethylenediaminetetraacetic acid,ethylenediaminetetra(methylenephosphonic acid) and water-soluble saltsthereof. Such catalysts are disclosed in U.S. Pat. No. 4,430,243.

If desired, the compositions herein can be catalyzed by means of amanganese compound. Such compounds and levels of use are well known inthe art and include, for example, the manganese-based catalystsdisclosed in U.S. Pat. No. 5,576,282.

Cobalt bleach catalysts useful herein are known, and are described, forexample, in U.S. Pat. No. 5,597,936; U.S. Pat. No. 5,595,967. Suchcobalt catalysts are readily prepared by known procedures, such astaught for example in U.S. Pat. No. 5,597,936, and U.S. Pat. No.5,595,967.

Compositions herein may also suitably include a transition metal complexof ligands such as bispidones (WO 05/042532 A1) and/or macropolycyclicrigid ligands—abbreviated as “MRLs”. As a practical matter, and not byway of limitation, the compositions and processes herein can be adjustedto provide on the order of at least one part per hundred million of theactive MRL species in the aqueous washing medium, and will typicallyprovide from about 0.005 ppm to about 25 ppm, from about 0.05 ppm toabout 10 ppm, or even from about 0.1 ppm to about 5 ppm, of the MRL inthe wash liquor.

Suitable transition-metals in the instant transition-metal bleachcatalyst include, for example, manganese, iron and chromium. SuitableMRLs include 5,12-diethyl-1,5,8,12-tetraazabicyclo[6.6.2]hexadecane.

Suitable transition metal MRLs are readily prepared by known procedures,such as taught for example in WO 00/32601, and U.S. Pat. No. 6,225,464.

Solvents—Suitable solvents include water and other solvents such aslipophilic fluids. Examples of suitable lipophilic fluids includesiloxanes, other silicones, hydrocarbons, glycol ethers, glycerinederivatives such as glycerine ethers, perfluorinated amines,perfluorinated and hydrofluoroether solvents, low-volatilitynonfluorinated organic solvents, diol solvents, otherenvironmentally-friendly solvents and mixtures thereof.

Processes of Making Compositions

The compositions of the present invention can be formulated into anysuitable form and prepared by any process chosen by the formulator,non-limiting examples of which are described in Applicants' examples andin U.S. Pat. No. 4,990,280; U.S. 20030087791A1; U.S. 20030087790A1; U.S.20050003983A1; U.S. 20040048764A1; U.S. Pat. No. 4,762,636; U.S. Pat.No. 6,291,412; U.S. 20050227891A1; EP 1070115A2; U.S. Pat. No.5,879,584; U.S. Pat. No. 5,691,297; U.S. Pat. No. 5,574,005; U.S. Pat.No. 5,569,645; U.S. Pat. No. 5,565,422; U.S. Pat. No. 5,516,448; U.S.Pat. No. 5,489,392; U.S. Pat. No. 5,486,303.

Method of Use

The present invention includes a method for cleaning and/or treating asitus inter alia a surface or fabric. Such method includes the steps ofoptionally washing and/or rinsing said surface or fabric, contactingsaid surface or fabric with a composition of the present invention inneat or diluted form such as in a wash liquor and then optionallywashing and/or rinsing said surface or fabric. For purposes of thepresent invention, washing includes but is not limited to, scrubbing,and mechanical agitation. As will be appreciated by one skilled in theart, the cleaning compositions of the present invention are ideallysuited for use in laundry applications. Accordingly, the presentinvention includes a method for laundering a fabric. The method maycomprise the steps of contacting a fabric to be laundered with a saidcleaning laundry solution comprising at least one embodiment ofApplicants' cleaning composition, cleaning additive or mixture thereof.The fabric may comprise most any fabric capable of being laundered innormal consumer use conditions. The solution may have in one aspect a pHof from about 7.5 to about

10.5 or even a pH of from about 8 to about 10.5. The compositions may beemployed at

concentrations of from about 500 ppm to about 15,000 ppm in solution.The water temperatures typically range from about 5° C. to about 90° C.The water to fabric ratio is typically from about 1:1 to about 30:1.

Test Methods Test Method 1 Procedure for Determining the Concentrationof Free CALCIUM (Ca⁺⁺) Basis of Method

Free calcium is assayed by using an ion specific electrode that isspecific for calcium. This measurement technique is well known and isexemplified in many literature references, such as Analytical Chemistry,Vol 46, No 1, 1974, p. 12-15, and manuals exemplifying the use of suchelectrodes are broadly known and available (e.g. from Metrohm ofBuckinghamshire, UK and from HACH LANGE LTD, Manchester, UK). Thedescription below shows how such a technique may be applied tomeasurements of free calcium for detergents.

Calibration:

Before use, the electrodes must be calibrated. This may be done bymeasuring a series of known standard solutions, made by serial dilutionof the 1000 ppm Calcium standard solution. For a full calibration,prepare 100 ml of solutions containing 1000, 100, 10, 1, and 0.1 ppmCa²⁺.

Add 2 ml of Ionic Strength Adjustment Buffer (ISAB) solution to eachstandard and mix. Prepare a calibration graph.

Sample Preparation

-   -   a. To 6 separate IL volumetric flasks add, 0, 20, 30, 40, 50,        100 and 200 ml of 1000 ppm calcium standard solution and add        deionised water to make the volume to 1 liter to make solutions        containing 0, 20, 30, 40, 50, 100 & 200 ppm of calcium. Transfer        each 1 liter calcium solution to a 1 liter tergotometer pot and        stir for 10 mins on a standard tergotometer.    -   b. To 50 ml of each solution from Step a. above, add 1 ml of        ISAB buffer and measure calcium. This serves to check that the        initial solution contains the level of calcium expected.    -   c. To each tergotometer pot from Step a. above add sufficient        detergent to give a detergent solution having the same        concentration as would be realized by adding the detergent        manufacturer's recommended dose of detergent to the standard        volume within a washing machine or median hand-wash practices.        (For example formulations 1-6, typical detergent concentration        would be 1.5-3 g/liter; for example formulations 7-12, typical        detergent concentration would be 8-9 g/liter; for example        formulations 13-16, typical detergent concentration would be 1.5        g/liter; and for examples 17 & 18, typical detergent        concentrations would be 8-9 g/liter). Stir for 10 mins.    -   d. To 50 ml of each solution from Step c., add 1 ml of ISAB        buffer, immerse the electrode and take the calcium reading, once        equilibrated (typically takes several seconds). This is the free        calcium reading for the detergent composition.

Apparatus Used:

Ion-Selective Calcium Electrode: Ion-selective calcium electrodes arebroadly available. The one used for this test is sourced from VWRInternational Ltd., Leicestershire, UK and comprises the followingparts: Ion-Selective Electrode for calcium ion (such as ELIT 8041 PVCmembrane); Reference electrode: single junction silver chloride (such asELIT 001); Dual electrode head (such as ELIT 201); ELIT ComputerInterface/Ion Analyzer attached to a Dell PC.

Standard solutions: The 1000 ppm calcium chloride solution can be madeby dissolving calcium chloride (sourced from Sigma Aldrich of Milwaukee,US) in deionized water, and the buffer solution (ISAB) comprising 4Molar KCl can be sourced from VWR International Ltd., Leicestershire,UK.

Standard Tergotometer: (e.g. models available from Copley Scientific,Nottingham, UK such as that sold under catalogue number DissolutionTester DIS 8000).

Test Method 2 Procedure for Determining Enzyme Deposition Index Basis ofMethod:

This method compares the residual enzyme concentration of variousamylases detectable by standard Double Antibody Sandwich ELISA(DAS-ELISA) methods, well known to those skilled in the art, by reactionwith the appropriate antibodies (DAS-ELISA technique is exemplified invarious patents, e.g. U.S. Pat. No. 5,188,937 & U.S. Pat. No. 6,818,804,and in various literature articles, e.g. L. S. Miller, “A roboticimmunoassay system for detergent enzymes.” Laboratory InformationManagement, 1994, Vol 26, pgs 79-87; Butler, J. E. “The immunochemistryof sandwich ELISA's: principles and applications for the quantitativedetermination of immunoglobulins.” In “ELISA and Other Solid PhaseImmunoassays. Theoretical and Practical Aspects” Eds Kemeny, D. M. andChallacombe, S. J. John Wiley and Sons, NY. 1988, pgs. 155-180 andreferences incorporated therein.) Standard calibration methods are used.

The enzyme deposition index (EDI) is the ratio of the (mass of testalpha-amylase protein extracted/g fabric) and the (mass of Termamyl®protein extracted/g fabric). Thus, the equation for cotton fabric isEquation 1. This method may be used, for example, to determine thesuitability of an enzyme for use as a detergent ingredient and/orpredict the performance of an enzyme in, for example, a detergentapplication.

EDI=(Mass of test alpha-amylase protein extracted per g cotton)/(Mass ofTermamyl® extracted per g cotton)  Equation 1

Sample Preparation

-   -   1. To separate tergotometer pots add 980 ml of water containing        145±10 ppm calcium and 2.0 g of sodium carbonate (sourced from        SigmaAldrich of Milwaukee, USA). Stir for 10 minutes to        dissolve. Allow to equilibrate to 40° C.    -   2. Add 0.69 g of LAS (Linear alkylbenzenesulfonate having an        average aliphatic carbon chain length C₁₁-C₁₂) and 0.38 g of        AE3S(C₁₂₋₁₅ alkyl ethoxy (3) sulfate), both supplied by Stepan,        Northfield, Ill., USA. Stir to dissolve.    -   3. Add liquid samples of the various enzymes to be studied to        the different tergotometer pots to ensure 0.2 mg of amylase are        present in each pot. One pot should contain 0.2 mg Termamyl®        (available from Novozymes of Denmark) to act as the reference        versus which the other enzymes are to be indexed.    -   4. Adjust the water volume in each pot to 1 liter, if needed,        using water containing 145±10 ppm calcium. The resultant        solution should contain 690 ppm of LAS, 380 ppm AE3S, 2000 ppm        of sodium carbonate and 0.2 ppm of the enzyme.    -   5. To each tergotometer pot, add three standard cotton swatches        (sourced ex. Center for Test Materials (CFT) B.V. of Holland)        with fabric code CN03, each weighing 3.5±0.3 g. The total weight        of cotton should be 10.5±0.5 g per tergotometer pot.    -   6. Start the tergotometer run (conditions are 40±2° C., 150 rpm        and run time is 20 minutes).    -   7. After 20 minutes the fabrics are removed, hand squeezed until        not excess liquid is visible and then rinsed for 5 minutes in a        tergotometer in 1 liter of water containing 145±10 ppm calcium        (conditions are 150 rpm agitation, with a water temperature of        25±2° C.).    -   8. The swatches are removed and hand squeezed to remove excess        liquor and then allowed to air dry at room temperature for 3-5        hours.    -   9. An extraction buffer is prepared comprising of:        -   a. 0.93 g/L 2-Amino-2-(hydroxymethyl)-1,3-propanediol            (otherwise known as Trizma base);        -   b. 4.96 g/L Sodium Thiosulphate pentahydrate;        -   c. 0.147 g/L Calcium Chloride dehydrate;        -   d. 29.22 g/L sodium Chloride;        -   e. 1.0 g Sodium Azide; and        -   f. 1.0 g/L Polyethylene glycol sorbitan monolaurate            (otherwise known as Tween 20 with CAS #9005-64-5)        -   The pH of the buffer is adjusted to pH=8 using 0.1N            hydrochloric acid prior to use.        -   All reagents are available from Sigma Aldrich Company Ltd.            Dorset, UK.    -   10. Each swatch of known weight is placed in a separate 50 ml        extraction tube and 25 ml of extraction buffer is added. The        tube is hand shaken vigorously for 1 minute (+/−10 s) then left        to stand for 15 minutes (+/−1 minute) then shaken vigorously        again for 1 minute (+/−10 s). The tube is allowed to stand for a        further 15 minutes (+/−1 minute) before given a final vigorous        shaking for 1 minute (+/−10 s).    -   11. The resultant solution is assayed via standard ELISA methods        using a Rosys Plato 7381 analyzer (Supplier Rosys Anthos GmbH        Feldbachstr CH-8634 Hombrechtikon Switzerland or equivalent        ELISA equipment such as those supplied by Dynex Technologies of        Virginia, USA or Biotech of Vermont, USA).    -   12. From this assay by comparing to the standard calibration        curve, the mass of amylase protein detected can be determined        and the mass of enzyme extracted/g of fabric can be calculated.    -   13. The whole process (Steps 1-12) is repeated 3 more times to        generate further sets of data.    -   14. The enzyme deposition index is then calculated by taking the        average of 12 readings expressed in ng amylase protein/g fabric        (these twelve readings come from the three pieces of cloth per        pot from each of the four runs) for each enzyme and indexing        such value to that observed for Termamyl® protein as shown in        Equation 1.

Equipment Used

Standard Tergotometer (e.g. models available from Copley Scientific,Nottingham, UK such as that sold under catalogue number DissolutionTester DIS 8000).

EXAMPLES

Unless otherwise indicated, materials can be obtained from Aldrich, P.O.Box 2060, Milwaukee, Wis. 53201, USA.

Examples 1-6

Granular laundry detergent compositions designed for hand washing ortop-loading washing machines.

1 2 3 4 5 6 (wt %) (wt %) (wt %) (wt %) (wt %) (wt %) Linearalkylbenzenesulfonate 20 22 20 15 20 20 C₁₂₋₁₄ Dimethylhydroxyethyl 0.70.2 1 0.6 0.0 0 ammonium chloride AE3S 0.9 1 0.9 0.0 0.5 0.9 AE7 0.0 0.00.0 1 0.0 3 Sodium tripolyphosphate 5 0.0 4 9 2 0.0 Zeolite A 0.0 1 0.01 4 1 1.6R Silicate (SiO₂:Na₂O at 7 5 2 3 3 5 ratio 1.6:1) SodiumCarbonate 25 20 25 17 18 19 Polyacrylate MW 4500 1 0.6 1 1 1.5 1 CarboxyMethyl Cellulose 1 0.3 1 1 1 1 Amylase* (20 mg active/g) 0.1 0.2 0.1 0.20.1 0.1 Savinase ® (32.89 mg active/g) 0.1 0.1 0.1 0.1 0.1 0.1Natalase ® (8.65 mg active/g) 0.1 0.0 0.1 0.0 0.1 0.1 Lipex ® (18 mgactive/g) 0.03 0.07 0.3 0.1 0.07 0.4 Fluorescent Brightener 1 0.06 0.00.06 0.18 0.06 0.06 Fluorescent Brightener 2 0.1 0.06 0.1 0.0 0.1 0.1DTPA 0.6 0.8 0.6 0.25 0.6 0.6 MgSO₄ 1 1 1 0.5 1 1 Sodium Percarbonate0.0 5.2 0.1 0.0 0.0 0.0 Sodium Perborate 4.4 0.0 3.85 2.09 0.78 3.63Monohydrate NOBS 1.9 0.0 1.66 0.0 0.33 0.75 TAED 0.58 1.2 0.51 0.0 0.0150.28 Sulphonated zinc 0.0030 0.0 0.0012 0.0030 0.0021 0.0 phthalocyanineS-ACMC 0.1 0.0 0.0 0.0 0.06 0.0 Direct Violet 9 0.0 0.0 0.0003 0.00050.0003 0.0 Acid Blue 29 0.0 0.0 0.0 0.0 0.0 0.0003 Sulfate/Moisture**Balance to 100% for Examples 1-6

Examples 7-12

Granular laundry detergent compositions designed for front-loadingautomatic washing machines.

7 8 9 10 11 12 (wt %) (wt %) (wt %) (wt %) (wt %) (wt %) Linearalkylbenzenesulfonate 8 7.1 7 6.5 7.5 7.5 AE3S 0 4.8 0 5.2 4 4Alkylsulfate 1 0 1 0 0 0 AE7 2.2 0 3.2 0 0 0 C₁₀₋₁₂ Dimethyl 0.75 0.940.98 0.98 0 0 hydroxyethylammonium chloride Crystalline layered silicate(δ- 4.1 0 4.8 0 0 0 Na₂Si₂O₅) Zeolite A 5 0 5 0 2 2 Citric Acid 3 5 3 42.5 3 Sodium Carbonate 15 20 14 20 23 23 Silicate 2R (SiO₂:Na₂O at ratio0.08 0 0.11 0 0 0 2:1) Soil release agent 0.75 0.72 0.71 0.72 0 0Acrylic Acid/Maleic Acid 1.1 3.7 1.0 3.7 2.6 3.8 CopolymerCarboxymethylcellulose 0.15 1.4 0.2 1.4 1 0.5 Protease (84 mg active/g)0.2 0.2 0.3 0.15 0.12 0.13 Amylase* (20 mg active/g) 0.2 0.15 0.2 0.30.15 0.15 Lipex ® (18.00 mg active/g) 0.05 0.15 0.1 0 0 0 Natalase ®(8.65 mg active/g) 0.1 0.2 0 0 0.15 0.15 Celluclean ™ (15.6 mg active/g)0 0 0 0 0.1 0.1 TAED 3.6 4.0 3.6 4.0 2.2 1.4 Percarbonate 13 13.2 1313.2 16 14 Na salt of Ethylenediamine-N,N′- 0.2 0.2 0.2 0.2 0.2 0.2disuccinic acid, (S,S) isomer (EDDS) Hydroxyethane di phosphonate 0.20.2 0.2 0.2 0.2 0.2 (HEDP) MgSO₄ 0.42 0.42 0.42 0.42 0.4 0.4 Perfume 0.50.6 0.5 0.6 0.6 0.6 Suds suppressor agglomerate 0.05 0.1 0.05 0.1 0.060.05 Soap 0.45 0.45 0.45 0.45 0 0 Sulphonated zinc phthalocyanine 0.00070.0012 0.0007 0 0 0 (active) S-ACMC 0.01 0.01 0 0.01 0 0 Direct Violet 9(active) 0 0 0.0001 0.0001 0 0 Sulfate/Water & Miscellaneous* *Balanceto 100% for Examples 7-12

Any of the above compositions is used to launder fabrics at aconcentration of 7000 to 10000 ppm in water, 20-90° C., and a 5:1water:cloth ratio. The typical pH is about 10.

Examples 13-18 Heavy Duty Liquid Laundry Detergent Compositions RawMaterials and Notes For Composition Examples 1-18

13 14 15 16 17 18 (wt %) (wt %) (wt %) (wt %) (wt %) (wt %) AES C₁₂₋₁₅alkyl 11 10 4 6.32 0 0 ethoxy (1.8) sulfate AE3S 0 0 0 0 2.4 0 Linearalkyl 1.4 4 8 3.3 5 8 benzene sulfonate HSAS 3 5.1 3 0 0 0 Sodiumformate 1.6 0.09 1.2 0.04 1.6 1.2 Sodium hydroxide 2.3 3.8 1.7 1.9 1.72.5 Monoethanolamine 1.4 1.49 1.0 0.7 0 0 Diethylene glycol 5.5 0.0 4.10.0 0 0 Nonionic 23.9 0.4 0.6 0.3 0.3 0 0 Nonionic 24.7 0 0 0 0 2.4 6Chelant 0.15 0.15 0.11 0.07 0.5 0.11 Citric Acid 2.5 3.96 1.88 1.98 0.92.5 C₁₂₋₁₄ dimethyl 0.3 0.73 0.23 0.37 0 0 Amine Oxide C₁₂₋₁₈ Fatty Acid0.8 1.9 0.6 0.99 3.5 2.5 Borax 1.43 1.5 1.1 0.75 1 1.07 Ethanol 1.541.77 1.15 0.89 0 3 Ethoxylated (EO₁₅) 0.3 0.33 0.23 0.17 0.0 0.0tetraethylene pentaimine¹ Ethoxylated 0.8 0.81 0.6 0.4 1 1 hexamethylenediamine² 1,2-Propanediol 0.0 6.6 0.0 3.3 0.5 2 Protease (40.6 mgactive/g) 0.8 0.6 0.7 0.9 0.7 0.6 Mannaway ® (25 mg active/g) 0.07 0.050.045 0.06 0.04 0.045 Amylase* (15 mg active/g) 0.3 0.2 0.3 0.1 0.2 0.4Natalase ® (29 mg 0 0.2 0.1 0.15 0.07 0 active/g) Lipex ® (18 mgactive/g) 0.4 0.2 0.3 0.1 0.2 0 Liquitint ® Violet 0.006 0.002 0 0 00.002 CT (active) S-ACMC — — 0.01 0.05 0.01 0.02 Water, perfume, dyes &Balance Balance Balance Balance Balance Balance other components

Raw Materials and Notes For Composition Examples 1-18

Linear alkylbenzenesulfonate having an average aliphatic carbon chainlength C₁₁-C₁₂ supplied by Stepan, Northfield, Ill., USA

C₁₂₋₁₄ Dimethylhydroxyethyl ammonium chloride, supplied by ClariantGmbH, Sulzbach, Germany

-   -   AE3S is C₁₂₋₁₅ alkyl ethoxy (3) sulfate supplied by Stepan,        Northfield, Ill., USA

AE7 is C₁₂₋₁₅ alcohol ethoxylate, with an average degree of ethoxylationof 7, supplied by Huntsman, Salt Lake City, Utah, USA

Sodium tripolyphosphate is supplied by Rhodia, Paris, France

Zeolite A is supplied by Industrial Zeolite (UK) Ltd, Grays, Essex, UK

1.6R Silicate is supplied by Koma, Nestemica, Czech Republic

Sodium Carbonate is supplied by Solvay, Houston, Tex., USA

Polyacrylate MW 4500 is supplied by BASF, Ludwigshafen, Germany

Carboxy Methyl Cellulose is Finnfix® BDA supplied by CP Kelco, Arnhem,Netherlands

Suitable chelants are, for example, diethylenetetraamine pentaaceticacid (DTPA) supplied by Dow Chemical, Midland, Mich., USA orHydroxyethane di phosphonate (HEDP) supplied by Solutia, St Louis, Mo.,USA Bagsvaerd, Denmark

Protease (examples 7-12) described in U.S. Pat. No. 6,312,936 B1supplied by Genencor International, Palo Alto, Calif., USA

Protease (examples 13-18) described in U.S. Pat. No. 4,760,025 issupplied by Genencor International, Palo Alto, Calif., USA

-   -   A suitable amylase is, for example, Optisize® HT Plus supplied        by Genencor International, Palo Alto, Calif., USA, or any of the        other amylases specifically described in the present        specification.

Fluorescent Brightener 1 is Tinopal® AMS, Fluorescent Brightener 2 isTinopal® CBS-X, Sulphonated zinc phthalocyanine and Direct Violet 9 isPergasol® Violet BN-Z all supplied by Ciba Specialty Chemicals, Basel,Switzerland

Sodium percarbonate supplied by Solvay, Houston, Tex., USA

Sodium perborate is supplied by Degussa, Hanau, Germany

NOBS is sodium nonanoyloxybenzenesulfonate, supplied by Eastman,Batesville, Ark., USA

TAED is tetraacetylethylenediamine, supplied under the Peractive® brandname by Clariant GmbH, Sulzbach, Germany

S-ACMC is carboxymethylcellulose conjugated with C.I. Reactive Blue 19,sold by Megazyme, Wicklow, Ireland under the product nameAZO-CM-CELLULOSE, product code S-ACMC.

Soil release agent is Repel-o-tex® PF, supplied by Rhodia, Paris, France

Acrylic Acid/Maleic Acid Copolymer is molecular weight 70,000 andacrylate:maleate ratio 70:30, supplied by BASF, Ludwigshafen, Germany

Na salt of Ethylenediamine-N,N′-disuccinic acid, (S,S) isomer (EDDS) issupplied by Octel, Ellesmere Port, UK

Hydroxyethane di phosphonate (HEDP) is supplied by Dow Chemical,Midland, Mich., USA

Suds suppressor agglomerate is supplied by Dow Corning, Midland, Mich.,USA

HSAS is mid-branched alkyl sulfate as disclosed in U.S. Pat. No.6,020,303 and U.S. Pat. No. 6,060,443

C₁₂₋₁₄ dimethyl Amine Oxide is supplied by Procter & Gamble Chemicals,Cincinnati, Ohio, USA

Liquitint(Violet CT is supplied by Milliken, Spartanburg, S.C., USA)

¹ as described in U.S. Pat. No. 4,597,898.

² available under the tradename LUTENSIT® from BASF and such as thosedescribed in WO 01/05874

The dimensions and values disclosed herein are not to be understood asbeing strictly limited to the exact numerical values recited. Instead,unless otherwise specified, each such dimension is intended to mean boththe recited value and a functionally equivalent range surrounding thatvalue. For example, a dimension disclosed as “40 mm” is intended to mean“about 40 mm”.

All documents cited in the Detailed Description of the Invention are, inrelevant part, incorporated herein by reference; the citation of anydocument is not to be construed as an admission that it is prior artwith respect to the present invention. To the extent that any meaning ordefinition of a term in this document conflicts with any meaning ordefinition of the same term in a document incorporated by reference, themeaning or definition assigned to that term in this document shallgovern.

While particular embodiments of the present invention have beenillustrated and described, it would be obvious to those skilled in theart that various other changes and modifications can be made withoutdeparting from the spirit and scope of the invention. It is thereforeintended to cover in the appended claims all such changes andmodifications that are within the scope of this invention.

1. A composition comprising an amylase having Seq. I.D. 1 and based ontotal product weight, less than 15% builder.
 2. The composition of claim1, said composition comprising a material selected from the groupconsisting of surfactants, chelating agents, dye transfer inhibitingagents, dispersants, additional enzymes, and enzyme stabilizers,catalytic materials, bleaching agents, polymeric dispersing agents, claysoil removal/anti-redeposition agents, brighteners, suds suppressors,dyes, perfumes, structure elasticizing agents, fabric softeners,carriers, hydrotropes, processing aids, solvents, pigments, hueingagents, photobleaches, structurants, and mixtures thereof.
 3. Thecomposition of claim 2, said composition comprising an additionalenzyme.
 4. The composition of claim 3, wherein said additional enzyme isselected from the group consisting of hemicellulases, peroxidases,proteases, cellulases, xylanases, lipases, phospholipases, esterases,cutinases, pectinases, mannanases, pectate lyases, keratinases,reductases, oxidases, phenoloxidases, lipoxygenases, ligninases,pullulanases, tannases, pentosanases, glucanases, arabinosidases,hyaluronidase, chondroitinase, laccase, amylases, and mixtures thereof.5. The composition of claim 4, wherein said additional enzyme isselected from the group consisting of: a.) lipases; b.) alpha-amylases;c.) serine proteases; d.) microbial-derived endoglucanases; and e.)mixtures thereof.
 6. The composition of claim 2, said compositioncomprising a surfactant, selected from the group of: a.) anionicsurfactants selected from the group consisting of linearalkylbenzene-sulfonate (LAS), alcohol ethoxysulfate (AES), mid-branchedalkyl sulfates (HSAS) and mixtures thereof; b.) non ionic alcoholethoxylates, said alcohol ethoxylates; c.) amine oxides; and d.)mixtures thereof.
 7. The composition of claim 2, said compositioncomprising a polymer, selected from the group consisting of a.)polyacrylates; b.) maleic/acrylic acid copolymers; c.) cellulose-derivedpolymers; d.) polyethyleneimine polymer; and e.) mixtures thereof. 8.The composition of claim 2, said composition comprising a materialselected from the group consisting of a photobleach, a fabric hueingagent and mixtures thereof, said photobleach being selected from thegroup consisting of a.) xanthene dyes; b.) sulfonated zincphthalocyanine, sulfonated aluminum phthalocyanine, Eosin Y, Phoxine B,Rose Bengal, C.I. Food Red 14 and mixtures thereof; c.) water solublephthalocyanine; and d.) mixtures thereof and said fabric hueing agentbeing selected from the group consisting of a.) dyes; b.) dye-clayconjugates comprising at least one cationic/basic dye and a smectiteclay; and c.) mixtures thereof.
 9. The composition of claim 8, saidcomposition comprising, based on total product weight, from about 0% toabout 3% photobleach and/or from about 0.00003% to about 0.3% hueingagent.
 10. A composition comprising an amylase enzyme having E.C.3.2.1.1, and a material selected from the group consisting ofsurfactants, chelating agents, dye transfer inhibiting agents,dispersants, additional enzymes, and enzyme stabilizers, catalyticmaterials, bleaching agents, polymeric dispersing agents, clay soilremoval/anti-redeposition agents, brighteners, suds suppressors, dyes,perfumes, structure elasticizing agents, fabric softeners, carriers,hydrotropes, processing aids, solvents, pigments, hueing agents,photobleaches, structurants, and mixtures thereof, said compositionhaving an enzyme deposition index of at least 2.5.
 11. The compositionof claim 10, said composition comprising an additional enzyme.
 12. Thecomposition of claim 11, wherein said additional enzyme is selected fromthe group consisting of hemicellulases, peroxidases, proteases,cellulases, xylanases, lipases, phospholipases, esterases, cutinases,pectinases, mannanases, pectate lyases, keratinases, reductases,oxidases, phenoloxidases, lipoxygenases, ligninases, pullulanases,tannases, pentosanases, glucanases, arabinosidases, hyaluronidase,chondroitinase, laccase, amylases, or mixtures thereof.
 13. Thecomposition of claim 12, wherein said additional enzyme is selected fromthe group consisting of: a.) lipases; b.) alpha-amylases; c.) serineproteases; d.) microbial-derived endoglucanases; and e.) mixturesthereof.
 14. The composition of claim 10, said composition comprising asurfactant, selected from the group of: a.) anionic surfactants selectedfrom the group consisting of linear alkylbenzene-sulfonate (LAS),alcohol ethoxysulfate (AES), mid-branched alkyl sulfates (HSAS) andmixtures thereof; b.) non ionic alcohol ethoxylates; c.) amine oxides;and d.) mixtures thereof.
 15. The composition of claim 10, saidcomposition comprising a polymer selected from the group consisting of:a.) polyacrylates; b.) maleic/acrylic acid copolymers; c.)cellulose-derived polymers; d.) polyethyleneimine polymer; and e.)mixtures thereof.
 16. The composition of claim 10, said compositioncomprising a builder selected from the group consisting of a.) citricacid; b.) C₁₂-C₁₈ fatty acid; c.) aluminosilicates; d.) sodiumtripolyphosphate; and e.) mixtures thereof.
 17. The composition of claim16, said composition comprising, based on total product weight, lessthan 15% builder.
 18. The composition of claim 10, said compositioncomprising a material selected from the group consisting of aphotobleach, a hueing agent and mixtures thereof, said photobleach beingselected from the group consisting of a.) xanthene dyes; b.) sulfonatedzinc phthalocyanine, sulfonated aluminum phthalocyanine, Eosin Y,Phoxine B, Rose Bengal, C.I. Food Red 14 and mixtures thereof; c.) watersoluble phthalocyanine; and d.) mixtures thereof and said fabric hueingagent being selected from the group consisting of a.) dyes; b.) dye-clayconjugates comprising at least one cationic/basic dye and a smectiteclay; and c.) mixtures thereof.
 19. The composition of claim 18, saidcomposition comprising, based on total product weight, from about 0% toabout 3% photobleach and/or from about 0.00003% to about 0.3% hueingagent.
 20. A composition comprising an amylase having Seq. I.D. 1 and asufficient amount of calcium to provide a wash liquor comprising saidcomposition with a free calcium concentration of from about 0.1 ppm toabout 500 ppm.
 21. A method of determining the deposition index of anenzyme, said method comprising determining the enzyme deposition indexof an enzyme according to Test Method 2.